IED ID | IndEnz0002018569 |
Enzyme Type ID | protease018569 |
Protein Name |
Disintegrin and metalloproteinase domain-containing protein 10 homolog ADAM 10 homolog EC 3.4.24.81 |
Gene Name | sup-17 DY3.7 |
Organism | Caenorhabditis elegans |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
Enzyme Sequence | MSSPIRNRLQLVVTLIFCLFFENVNGLNNFIDNFETLNYRATHVANQVTRRKRSIDSAASHYQEPIGFRFNAYNRTFHVQLHPIDDSLFHEDHMSDVDGGYADIKPSHFLYEGYLKDDPNSHVHGSVFDGVFEGHIQTGEGRRYSIDKAAKYFERDDRPTQYHSIIYRDDEINHRKWRVKRDAENLSEQMQGCGFSSRVRREMTDVQNSGESTDFFTNYMTMGGRSKRANTLRDHDGLYFVRTCSLYMQADHKLYEHIRMKEGNNDPIRTREEIVSLFYNHIKAVNEIYEGTNFNGIKGLHFVIQRTSIYTPDSCDRGRAKTDSDNPFCEENVDVSNFLNLNSQRNHSAFCLAYALTFRDFVGGTLGLAWVASPQFNTAGGICQVHQRYNEGSRGWVYRSLNTGIVTLVNYGNRVPARVSQLTLAHEIGHNFGSPHDFPAECQPGLPDGNFIMFASATSGDKPNNGKFSPCSVKNISAVLAVVLKSMPVDPTRNASPVGIGKRNCFQERTSAFCGNQIYEPGEECDCGFSQADCDQMGDKCCVPHEARGNGGPGPCKRKPGAQCSPSQGYCCNPDTCSLHGKNEEKICRQESECSNLQTCDGRNAQCPVSPPKHDGIPCQDSTKVCSSGQCNGSVCAMFGLEDCFLTEGKADELCFLACIKDGKCTSSVHLPEFSANRTNFLQNMRKDKPGLILHPGSPCNNYKGYCDIFRKCRSVDANGPLARLKNLLFNKRTIETLTQWAQDNWWVVGVGGLVFLVIMALFVKCCAVHTPSTNPNKPPALNIYQTLTRPGTLIRQHRQRHRAAAGSVPPGPGAQPRSGAASAPSRTTPSARPSAPPLVAPQVAVAVPPGVVGPPIPLIATHPGSSSSTPAVIVLEPPPPYTAADPGSAMGGPRRGHRKNKRQTSSDAAGSSGNGGKKKGK |
Enzyme Length | 922 |
Uniprot Accession Number | G5EFD9 |
Absorption | |
Active Site | ACT_SITE 427; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endopeptidase of broad specificity.; EC=3.4.24.81; Evidence={ECO:0000250|UniProtKB:O14672}; |
DNA Binding | |
EC Number | 3.4.24.81 |
Enzyme Function | FUNCTION: Metalloprotease (By similarity). Acts together with protease adm-4 and in a cell autonomous manner to facilitate lin-12/Notch signaling during developmental cell fate decision, including anchor cell/ventral uterine precursor cell decision and vulva precursor cell specification (PubMed:9428412, PubMed:9409830, PubMed:16197940). By modulating glp-1/Notch signaling, plays a role in germline development (PubMed:16197940). Probably by modulating BMP-like Sma/Mab signaling via the shedding of unc-40 ectodomain, involved in the regulation of body size and mesoderm development (PubMed:28068334). Probably by shedding ephrin efn-4, regulates axon guidance of SDQL neuron during development (PubMed:26903502). {ECO:0000250|UniProtKB:O14672, ECO:0000269|PubMed:16197940, ECO:0000269|PubMed:26903502, ECO:0000269|PubMed:28068334, ECO:0000269|PubMed:9409830, ECO:0000269|PubMed:9428412}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Disulfide bond (10); Domain (2); Glycosylation (6); Metal binding (3); Mutagenesis (2); Propeptide (1); Region (2); Signal peptide (1); Topological domain (2); Transmembrane (1) |
Keywords | Cell membrane;Cleavage on pair of basic residues;Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28068334}; Single-pass type I membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000269|PubMed:28068334}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:28068334}; Single-pass type I membrane protein {ECO:0000305}. Note=Localizes to the basolateral cell membrane in embryos. {ECO:0000269|PubMed:28068334}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 11559592; 17897480; 21085631; 21177967; 22004469; 22286215; 22500807; 22560298; 23800452; 25487147; 28669545; |
Motif | |
Gene Encoded By | |
Mass | 101,573 |
Kinetics | |
Metal Binding | METAL 426; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 430; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276; METAL 436; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276 |
Rhea ID | |
Cross Reference Brenda |